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Protein

Small conductance calcium-activated potassium channel protein 2

Gene

Kcnn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.3 Publications

GO - Molecular functioni

  • calmodulin binding Source: GO_Central
  • ion channel activity Source: MGI
  • small conductance calcium-activated potassium channel activity Source: UniProtKB

GO - Biological processi

  • ion transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-MMU-1296052. Ca2+ activated K+ channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Small conductance calcium-activated potassium channel protein 2
Short name:
SK2
Short name:
SKCa 2
Short name:
SKCa2
Alternative name(s):
KCa2.2
Gene namesi
Name:Kcnn2
Synonyms:Sk2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:2153182. Kcnn2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei398 – 41821Helical; Name=Segment S1Sequence analysisAdd
BLAST
Transmembranei428 – 44821Helical; Name=Segment S2Sequence analysisAdd
BLAST
Transmembranei474 – 49421Helical; Name=Segment S3Sequence analysisAdd
BLAST
Transmembranei516 – 53621Helical; Name=Segment S4Sequence analysisAdd
BLAST
Transmembranei565 – 58521Helical; Name=Segment S5Sequence analysisAdd
BLAST
Intramembranei605 – 62521Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Transmembranei634 – 65421Helical; Name=Segment S6Sequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: Ensembl
  • dendritic spine Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • neuronal cell body Source: GO_Central
  • plasma membrane Source: MGI
  • sarcolemma Source: UniProtKB
  • smooth endoplasmic reticulum Source: MGI
  • T-tubule Source: BHF-UCL
  • Z disc Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 839839Small conductance calcium-activated potassium channel protein 2PRO_0000155011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei420 – 4201PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP58390.
PaxDbiP58390.
PRIDEiP58390.

PTM databases

iPTMnetiP58390.

Expressioni

Tissue specificityi

Expressed in atrial and ventricular myocytes with higher levels in atrial myocytes (at protein level). Highly expressed in brain, liver and colon with low levels in kidney and testis. In colon, detected in smooth muscle cells.3 Publications

Gene expression databases

BgeeiP58390.
ExpressionAtlasiP58390. baseline and differential.
GenevisibleiP58390. MM.

Interactioni

Subunit structurei

Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067884.

Structurei

3D structure databases

ProteinModelPortaliP58390.
SMRiP58390. Positions 655-785.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni672 – 74877Calmodulin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi72 – 765Poly-Pro
Compositional biasi84 – 907Poly-Gln
Compositional biasi170 – 1745Poly-Cys
Compositional biasi237 – 25014His-richAdd
BLAST
Compositional biasi345 – 36622Gly-richAdd
BLAST
Compositional biasi823 – 8264Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3684. Eukaryota.
ENOG410XT9D. LUCA.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000276908.
HOVERGENiHBG052241.
InParanoidiP58390.
KOiK04943.
OMAiMESYDKH.
OrthoDBiEOG73FQMC.
TreeFamiTF315015.

Family and domain databases

InterProiIPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
IPR013099. K_chnl_dom.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 2 hits.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.

Sequencei

Sequence statusi: Complete.

P58390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIVLVRPTN RTRRLDSTGA GMGPSSHQQQ ESPLPTITHC AGCTTAWSPC
60 70 80 90 100
SFNSSDMETP LQFQRGFFPE QPPPPPRSSH LHCQQQQQSQ DKPCAPFAPL
110 120 130 140 150
PHPHHHPHLA HQQPGSGGSS PCLRCNSCAS SGAPAAGAGA GDNLSLLLRT
160 170 180 190 200
SSPGGAFRTR TSSPLSGSSC CCCCSSRRGS QLNVSELTPS SHASALRQQY
210 220 230 240 250
AQQPASASQY HQCHSLQPAT SPTGSLGSLG SGPPLSHHHH HPHPAHHQHH
260 270 280 290 300
QPQARRESNP FTEIAMSSCR YNGGVMRPLS NLSSSRRNLQ EMDSEAQPLQ
310 320 330 340 350
PPASVVGGGG GASSPSAAAA ASSSAPEIVV SKPEHNNSNN LALYGTGGGG
360 370 380 390 400
STGGGGGGSG HGSSSGTKSS KKKNQNIGYK LGHRRALFEK RKRLSDYALI
410 420 430 440 450
FGMFGIVVMV IETELSWGAY DKASLYSLAL KCLISLSTII LLGLIIVYHA
460 470 480 490 500
REIQLFMVDN GADDWRIAMT YERIFFICLE ILVCAIHPIP GNYTFTWTAR
510 520 530 540 550
LAFSYAPSTT TADVDIILSI PMFLRLYLIA RVMLLHSKLF TDASSRSIGA
560 570 580 590 600
LNKINFNTRF VMKTLMTICP GTVLLVFSIS LWIIAAWTVR ACERYHDQQD
610 620 630 640 650
VTSNFLGAMW LISITFLSIG YGDMVPNTYC GKGVCLLTGI MGAGCTALVV
660 670 680 690 700
AVVARKLELT KAEKHVHNFM MDTQLTKRVK NAAANVLRET WLIYKNTKLV
710 720 730 740 750
KKIDHAKVRK HQRKFLQAIH QLRSVKMEQR KLNDQANTLV DLAKTQNIMY
760 770 780 790 800
DMISDLNERS EDFEKRIVTL ETKLETLIGS IHALPGLISQ TIRQQQRDFI
810 820 830
ETQMENYDKH VSYNAERSRS SSRRRRSSST APPTSSESS
Length:839
Mass (Da):91,604
Last modified:October 16, 2013 - v2
Checksum:i5FF152099CDC2885
GO

Sequence cautioni

The sequence AAI25476.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAI37657.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAM88568.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC28176.1 differs from that shown. Reason: Frameshift at position 3. Curated
The sequence BAE28732.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence EDL09992.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871Q → K in BAC28176 (PubMed:16141072).Curated
Sequence conflicti119 – 1191S → R in BAC28176 (PubMed:16141072).Curated
Sequence conflicti542 – 5421D → N in BAC28176 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033158 mRNA. Translation: BAC28176.1. Frameshift.
AK149082 mRNA. Translation: BAE28732.1. Different initiation.
AC099590 Genomic DNA. No translation available.
AC101593 Genomic DNA. No translation available.
AC121957 Genomic DNA. No translation available.
AC122852 Genomic DNA. No translation available.
CH466528 Genomic DNA. Translation: EDL09992.1. Sequence problems.
AY123778 mRNA. Translation: AAM88568.1. Different initiation.
BC125475 mRNA. Translation: AAI25476.1. Different initiation.
BC137656 mRNA. Translation: AAI37657.1. Different initiation.
AF357240 mRNA. Translation: AAK48901.1.
AF533008 mRNA. Translation: AAQ10283.1.
RefSeqiNP_001299834.1. NM_001312905.1.
NP_536713.1. NM_080465.2.
UniGeneiMm.411614.
Mm.458654.

Genome annotation databases

EnsembliENSMUST00000066890; ENSMUSP00000067884; ENSMUSG00000054477.
ENSMUST00000183850; ENSMUSP00000139350; ENSMUSG00000054477.
GeneIDi140492.
KEGGimmu:140492.
UCSCiuc008evd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033158 mRNA. Translation: BAC28176.1. Frameshift.
AK149082 mRNA. Translation: BAE28732.1. Different initiation.
AC099590 Genomic DNA. No translation available.
AC101593 Genomic DNA. No translation available.
AC121957 Genomic DNA. No translation available.
AC122852 Genomic DNA. No translation available.
CH466528 Genomic DNA. Translation: EDL09992.1. Sequence problems.
AY123778 mRNA. Translation: AAM88568.1. Different initiation.
BC125475 mRNA. Translation: AAI25476.1. Different initiation.
BC137656 mRNA. Translation: AAI37657.1. Different initiation.
AF357240 mRNA. Translation: AAK48901.1.
AF533008 mRNA. Translation: AAQ10283.1.
RefSeqiNP_001299834.1. NM_001312905.1.
NP_536713.1. NM_080465.2.
UniGeneiMm.411614.
Mm.458654.

3D structure databases

ProteinModelPortaliP58390.
SMRiP58390. Positions 655-785.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067884.

PTM databases

iPTMnetiP58390.

Proteomic databases

MaxQBiP58390.
PaxDbiP58390.
PRIDEiP58390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066890; ENSMUSP00000067884; ENSMUSG00000054477.
ENSMUST00000183850; ENSMUSP00000139350; ENSMUSG00000054477.
GeneIDi140492.
KEGGimmu:140492.
UCSCiuc008evd.1. mouse.

Organism-specific databases

CTDi3781.
MGIiMGI:2153182. Kcnn2.

Phylogenomic databases

eggNOGiKOG3684. Eukaryota.
ENOG410XT9D. LUCA.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000276908.
HOVERGENiHBG052241.
InParanoidiP58390.
KOiK04943.
OMAiMESYDKH.
OrthoDBiEOG73FQMC.
TreeFamiTF315015.

Enzyme and pathway databases

ReactomeiR-MMU-1296052. Ca2+ activated K+ channels.

Miscellaneous databases

PROiP58390.
SOURCEiSearch...

Gene expression databases

BgeeiP58390.
ExpressionAtlasiP58390. baseline and differential.
GenevisibleiP58390. MM.

Family and domain databases

InterProiIPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
IPR013099. K_chnl_dom.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 2 hits.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Sympathetic ganglion and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Cloning and expression of a small-conductance Ca(2+)-activated K+ channel from the mouse cochlea: coexpression with alpha9/alpha10 acetylcholine receptors."
    Nie L., Song H., Chen M.F., Chiamvimonvat N., Beisel K.W., Yamoah E.N., Vazquez A.E.
    J. Neurophysiol. 91:1536-1544(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-839, FUNCTION.
    Strain: C3H/HeJ.
    Tissue: Cochlea.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-839.
    Tissue: Brain.
  6. "Molecular properties of small-conductance Ca2+-activated K+ channels expressed in murine colonic smooth muscle."
    Ro S., Hatton W.J., Koh S.D., Horowitz B.
    Am. J. Physiol. 281:G964-G973(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 266-839, FUNCTION, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Colon.
  7. "Molecular identification and functional roles of a Ca(2+)-activated K+ channel in human and mouse hearts."
    Xu Y., Tuteja D., Zhang Z., Xu D., Zhang Y., Rodriguez J., Nie L., Tuxson H.R., Young J.N., Glatter K.A., Vazquez A.E., Yamoah E.N., Chiamvimonvat N.
    J. Biol. Chem. 278:49085-49094(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 266-839, FUNCTION, TISSUE SPECIFICITY.
    Strain: CD-1.
    Tissue: Heart.
  8. "Differential expression of small-conductance Ca2+-activated K+ channels SK1, SK2, and SK3 in mouse atrial and ventricular myocytes."
    Tuteja D., Xu D., Timofeyev V., Lu L., Sharma D., Zhang Z., Xu Y., Nie L., Vazquez A.E., Young J.N., Glatter K.A., Chiamvimonvat N.
    Am. J. Physiol. 289:H2714-H2723(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKCNN2_MOUSE
AccessioniPrimary (citable) accession number: P58390
Secondary accession number(s): E9QNY5
, Q3UF29, Q540U9, Q8CCH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 16, 2013
Last modified: July 6, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.